Conserved Pro-Glu (PE) and Pro-Pro-Glu (PPE) Protein Domains Target LipY Lipases of Pathogenic Mycobacteria to the Cell Surface via the ESX-5 Pathway

M.H. Daleke, A. Cascioferro, K. de Punder, R. Ummels, A.M. Abdallah, N. Wel, P.J. Peters, S. Luirink, R. Manganelli, W. Bitter

Research output: Contribution to JournalArticleAcademicpeer-review

Abstract

The type VII secretion system ESX-5 is a major pathway for export of PE and PPE proteins in pathogenic mycobacteria. These mycobacteria-specific protein families are characterized by conserved N-terminal domains of 100 and 180 amino acids, which contain the proline-glutamic acid (PE) and proline-proline-glutamic acid (PPE) motifs after which they are named. Here we investigated secretion of the triacylglycerol lipase LipY, which in fast-growing mycobacteria contains a signal sequence, but in slow-growing species appears to have replaced the signal peptide with a PE or PPE domain. Selected LipY homologues were expressed in wild-type Mycobacterium marinum and its corresponding ESX-5 mutant, and localization of the proteins was investigated by immunoblotting and electron microscopy. Our study shows that Mycobacterium tuberculosis PE-LipY (LipY
LanguageEnglish
Pages19024-19034
JournalJournal of Biological Chemistry
Volume286
Issue number21
DOIs
Publication statusPublished - 2011

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prolylglutamic acid
Mycobacterium
Lipase
Proline
Glutamic Acid
Proteins
Protein Sorting Signals
Mycobacterium marinum
Protein Domains
Mutant Proteins

Cite this

Daleke, M.H. ; Cascioferro, A. ; de Punder, K. ; Ummels, R. ; Abdallah, A.M. ; Wel, N. ; Peters, P.J. ; Luirink, S. ; Manganelli, R. ; Bitter, W. / Conserved Pro-Glu (PE) and Pro-Pro-Glu (PPE) Protein Domains Target LipY Lipases of Pathogenic Mycobacteria to the Cell Surface via the ESX-5 Pathway. In: Journal of Biological Chemistry. 2011 ; Vol. 286, No. 21. pp. 19024-19034.
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abstract = "The type VII secretion system ESX-5 is a major pathway for export of PE and PPE proteins in pathogenic mycobacteria. These mycobacteria-specific protein families are characterized by conserved N-terminal domains of 100 and 180 amino acids, which contain the proline-glutamic acid (PE) and proline-proline-glutamic acid (PPE) motifs after which they are named. Here we investigated secretion of the triacylglycerol lipase LipY, which in fast-growing mycobacteria contains a signal sequence, but in slow-growing species appears to have replaced the signal peptide with a PE or PPE domain. Selected LipY homologues were expressed in wild-type Mycobacterium marinum and its corresponding ESX-5 mutant, and localization of the proteins was investigated by immunoblotting and electron microscopy. Our study shows that Mycobacterium tuberculosis PE-LipY (LipY",
author = "M.H. Daleke and A. Cascioferro and {de Punder}, K. and R. Ummels and A.M. Abdallah and N. Wel and P.J. Peters and S. Luirink and R. Manganelli and W. Bitter",
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Conserved Pro-Glu (PE) and Pro-Pro-Glu (PPE) Protein Domains Target LipY Lipases of Pathogenic Mycobacteria to the Cell Surface via the ESX-5 Pathway. / Daleke, M.H.; Cascioferro, A.; de Punder, K.; Ummels, R.; Abdallah, A.M.; Wel, N.; Peters, P.J.; Luirink, S.; Manganelli, R.; Bitter, W.

In: Journal of Biological Chemistry, Vol. 286, No. 21, 2011, p. 19024-19034.

Research output: Contribution to JournalArticleAcademicpeer-review

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AU - Bitter, W.

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AB - The type VII secretion system ESX-5 is a major pathway for export of PE and PPE proteins in pathogenic mycobacteria. These mycobacteria-specific protein families are characterized by conserved N-terminal domains of 100 and 180 amino acids, which contain the proline-glutamic acid (PE) and proline-proline-glutamic acid (PPE) motifs after which they are named. Here we investigated secretion of the triacylglycerol lipase LipY, which in fast-growing mycobacteria contains a signal sequence, but in slow-growing species appears to have replaced the signal peptide with a PE or PPE domain. Selected LipY homologues were expressed in wild-type Mycobacterium marinum and its corresponding ESX-5 mutant, and localization of the proteins was investigated by immunoblotting and electron microscopy. Our study shows that Mycobacterium tuberculosis PE-LipY (LipY

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